A novel dextran‐grafted tetrapeptide resin for antibody purification

Abstract

Short peptide biomimetic affinity chromatography as a novel antibody separation chromatography is a potential alternative to protein A chromatography. However, if directly attaching ligand to matrix, the adsorption capacity and mass transfer rate would be affected by pore blockage and steric effect. Grafting resin is an effective method to solve this problem by using polymer as a bridge between matrix and ligand. In this work, a novel resin was prepared by grafting a tetrapeptide to the dextran-grafted matrix. Then, the adsorption properties for human immunoglobin G and BSA were determined. The results showed the saturation adsorption capacity could reach to 133 mg/g resin at pH 8.9 with a significantly low dissociation constant (0.03 mg/mL). The influence of flow rates to dynamic binding capacity of this resin was less than that of the non-grafted resin. The separation performance of the resin showed monoclonal antibody could be well isolated from the Chinese hamster ovary culture supernatant at pH 9.0 with the purity of 93.0% and yield of 84.7% by one step. Overall, this resin could achieve higher binding capacity by the possible of gaining higher ligand density, indicating its potential significance for separation in larger scale systems.

Machine Learning Model for Biomimetic Chromatography Peptide Ligands

“…It is notable that the ML classifier was able to correctly categorize the peptide YFRH into Class A, which was later on developed to become part of a resin for affinity chromatography and exhibited good performance in purifying IgG. 31 Another study that was considered for external validation was from Wei et al 32 The study reports the development of 3 tetrapeptides for the purification of IgG. Because these peptides were experimentally found to be effective ligands for IgG purification, they are assumed to belong to Class A.…”

“…One of the peptides reported in the study, YYRY, was not included in the external validation because its Cruciani property values exceeded the range which was derived from the tetrapeptides used in this study (Figure S1). It is notable that the ML classifier was able to correctly categorize the peptide YFRH into Class A, which was later on developed to become part of a resin for affinity chromatography and exhibited good performance in purifying IgG . Another study that was considered for external validation was from Wei et al The study reports the development of 3 tetrapeptides for the purification of IgG.…”